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Infection and Immunity, March 2002, p. 1254-1259, Vol. 70, No. 3
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.3.1254-1259.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification of Major Outer Surface Proteins of Streptococcus agalactiae

Martin J. G. Hughes,1* Joanne C. Moore,1 Jonathan D. Lane,1 Rebecca Wilson,1,{dagger} Philippa K. Pribul,1 Zabin N. Younes,1 Richard J. Dobson,1,{ddagger} Paul Everest,1,§ Andrew J. Reason,2 Joanne M. Redfern,2 Fiona M. Greer,2 Thanai Paxton,3 Maria Panico,3 Howard R. Morris,2,3 Robert G. Feldman,1,4 and Joseph D. Santangelo1

Microscience Ltd.,1 M-Scan Ltd., Wokingham, Berks,2 Departments of Infectious Diseases,4 Biochemistry, Imperial School of Science, Medicine and Technology, Hammersmith Campus, London, United Kingdom3

Received 24 July 2001/ Returned for modification 25 September 2001/ Accepted 4 December 2001

To identify the major outer surface proteins of Streptococcus agalactiae (group B streptococcus), a proteomic analysis was undertaken. An extract of the outer surface proteins was separated by two-dimensional electrophoresis. The visualized spots were identified through a combination of peptide sequencing and reverse genetic methodologies. Of the 30 major spots identified as S. agalactiae specific, 27 have been identified. Six of these proteins, previously unidentified in S. agalactiae, were sequenced and cloned. These were ornithine carbamoyltransferase, phosphoglycerate kinase, nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase, purine nucleoside phosphorylase, enolase, and glucose-6-phosphate isomerase. Using a gram-positive expression system, we have overexpressed two of these proteins in an in vitro system. These recombinant, purified proteins were used to raise antisera. The identification of these proteins as residing on the outer surface was confirmed by the ability of the antisera to react against whole, live bacteria. Further, in a neonatal-animal model system, we demonstrate that some of these sera are protective against lethal doses of bacteria. These studies demonstrate the successful application of proteomics as a technique for identifying vaccine candidates.

* Corresponding author. Mailing address: 545 Eskdale Rd., Winnersh Triangle, Wokingham, Berks, RG41 5TU, United Kingdom. Phone: 44 118 9443321. Fax: 44 118 9443301. E-mail: m.hughes{at}microscience.com.

{dagger} Present address: Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, United Kingdom.

{ddagger} Present address: Department of Clinical Pharmacology, Queen Mary and Westfield College, London, United Kingdom.

§ Present address: Department of Veterinary Pathology, University of Glasgow, Glasgow, United Kingdom.

Infection and Immunity, March 2002, p. 1254-1259, Vol. 70, No. 3
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.3.1254-1259.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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